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. 1978 Jun 1;171(3):787–798. doi: 10.1042/bj1710787

Low-temperature kinetics of the reaction of oxygen and solubilized cytochrome oxidase.

B Chance, C Saronio, J S Leigh Jr, W J Ingledew, T E King
PMCID: PMC1184028  PMID: 208516

Abstract

The reaction of solubilized cytochrome oxidase in the fully reduced state with O2 at low temperatures reveals components with characteristics similar to those observed with the membrane-bound oxidase, namely compounds A and B, which are proposed to be 'oxy' and 'peroxy' compounds respectively. Similar species are identified in both solubilized and membrane-bound oxidases; the reaction velocity constant for the reation with O2 and the dissociation constant are decreased 2-3-fold in the solubilied preparation as compared with the membrane-bound species, owing to decreased reactivity towards O2 in the former. The oxidase prepared in the mixed-valence state shows the distinctive absorption band characteristic of compound C, identified in the membrane-bound oxidase. The assignment of the alpha, beta, gamma and near-i.r. absorption bands to possible valence states of these compounds is made.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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